INT148705

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.38
First Reported 2006
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 8
Total Number 13
Disease Relevance 5.19
Pain Relevance 1.81

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

extracellular space (TNFRSF1A) extracellular region (TNFRSF1A) plasma membrane (TNFRSF1A)
nucleus (TNFRSF1A) protein complex (TNFRSF1A)
Anatomy Link Frequency
somatic cell 1
T-cell 1
TNFRSF1A (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 3 99.90 Very High Very High Very High
Inflammation 98 98.00 Very High Very High Very High
Etanercept 30 94.60 High High
cytokine 44 94.36 High High
Inflammatory response 8 93.88 High High
Adalimumab 4 90.92 High High
Infliximab 5 90.32 High High
chemokine 14 82.56 Quite High
Arthritis 14 82.48 Quite High
spinal inflammation 88 74.88 Quite High
Disease Link Frequency Relevance Heat
Disease 67 99.82 Very High Very High Very High
Uveitis 123 98.88 Very High Very High Very High
INFLAMMATION 109 98.00 Very High Very High Very High
Hypercalcemia 1 95.24 Very High Very High Very High
Cancer 22 90.72 High High
Necrosis 15 90.60 High High
Acute-phase Reaction 1 89.64 High High
Apoptosis 12 89.20 High High
Autoimmune Disease 17 87.76 High High
Adhesions 2 87.16 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Similarly, HLA-B*27–positive patients with extraocular disease show an association with SNPs in the TNFRSF1A gene (TNFR1) compared to patients with AAU alone [21].
TNFR1 Binding (association) of associated with uveitis and disease
1) Confidence 0.38 Published 2009 Journal Molecular Vision Section Body Doc Link PMC2632733 Disease Relevance 1.04 Pain Relevance 0.12
Similarly, HLA-B*27–positive patients with extraocular disease show an association with SNPs in the TNFRSF1A gene (TNFR1) compared to patients with AAU alone [21].
TNFRSF1A Binding (association) of associated with uveitis and disease
2) Confidence 0.38 Published 2009 Journal Molecular Vision Section Body Doc Link PMC2632733 Disease Relevance 1.03 Pain Relevance 0.11
TNF interacts with two different receptors, designated TNFR1 and TNFR2, which are differentially expressed on cells and tissues and initiate both distinct and overlapping signal transduction pathways.
TNFR1 Binding (interacts) of
3) Confidence 0.28 Published 2008 Journal J. Pathol. Section Abstract Doc Link 18161752 Disease Relevance 0.86 Pain Relevance 0.15
Two recent studies have shown the potential of PMA, a PKC activator, to disrupt TNFR1 binding to these intermediates [42,50], however the study presented here is the first to show that this can be receptor mediated.
TNFR1 Binding (binding) of
4) Confidence 0.23 Published 2010 Journal Cellular Signalling Section Body Doc Link PMC2806525 Disease Relevance 0.07 Pain Relevance 0
We assessed the potential for PAR2 activation to disrupt the interaction of TNFR1 with a number of associated proteins.
TNFR1 Binding (interaction) of
5) Confidence 0.18 Published 2010 Journal Cellular Signalling Section Body Doc Link PMC2806525 Disease Relevance 0 Pain Relevance 0
TNFR1 was precipitated and the interaction with other proteins assessed by Western blotting.
TNFR1 Binding (interaction) of
6) Confidence 0.18 Published 2010 Journal Cellular Signalling Section Body Doc Link PMC2806525 Disease Relevance 0 Pain Relevance 0
Using the TNFR1/TRADD interaction as a model we pre-incubated cells with either GF109203X or YM254890 prior to PAR2 activating peptide pre-treatment.
TNFR1 Binding (interaction) of
7) Confidence 0.18 Published 2010 Journal Cellular Signalling Section Body Doc Link PMC2806525 Disease Relevance 0 Pain Relevance 0
driven TNFR1 and TRADD complex formation (Panel B).


TNFR1 Binding (formation) of
8) Confidence 0.17 Published 2010 Journal Cellular Signalling Section Body Doc Link PMC2806525 Disease Relevance 0 Pain Relevance 0
We also demonstrate for the first time receptor mediated driven disruption of TNFR1 binding to a number of associated proteins.
TNFR1 Binding (binding) of
9) Confidence 0.17 Published 2010 Journal Cellular Signalling Section Body Doc Link PMC2806525 Disease Relevance 0.08 Pain Relevance 0
This inflammatory pathway is initiated when TNF is cleaved from the cell surface by a specific metalloproteinase and binds to its two receptors, TNFR-55 and TNFR-75, found in both soluble forms and on somatic cell surfaces.
TNFR-55 Binding (binds) of in somatic cell associated with inflammation and metalloproteinase
10) Confidence 0.16 Published 2007 Journal Biologics : Targets & Therapy Section Body Doc Link PMC2721344 Disease Relevance 1.09 Pain Relevance 0.87
TNF-R/TNF interactions are critical for the clonal expansion/effector phases of immune responses, and involve DC/T-cell and B/T-cell interactions.
TNF-R Binding (interactions) of in T-cell
11) Confidence 0.12 Published 2007 Journal Biologics : Targets & Therapy Section Body Doc Link PMC2721321 Disease Relevance 0.06 Pain Relevance 0.03
can increase cellular ceramide levels via the de novo pathway as well as by binding to its membrane receptor (TNFR55), causing activation of neutral or acidic SMase [36,42,43].
TNFR55 Binding (binding) of
12) Confidence 0.08 Published 2006 Journal Arthritis Res Ther Section Body Doc Link PMC1779424 Disease Relevance 0.50 Pain Relevance 0.09
and prevents signaling through membrane-bound TNF-RI.
TNF-RI Binding (bound) of
13) Confidence 0.06 Published 2008 Journal Biologics : Targets & Therapy Section Body Doc Link PMC2727904 Disease Relevance 0.46 Pain Relevance 0.45

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox